acid-phosphatase and Poisoning

Sixteen male Suffolk lambs fed a 8 ppm Cu basal diet were randomly assigned to 2 groups: 12 copper-loaded (CL) and 4 controls (C). The CL sheep were drenched initially with 3 mg Cu/kg bw daily for a week. Every week an additional dose of 3 mg Cu/kg bw was included in the drench until signs of copper poisoning appeared; the control sheep were drenched with saline solution. The onset of copper poisoning occurred between 42 and 55 d. Food intake and body weight were recorded daily. Blood samples were collected weekly to measure the activity of the liver enzymes gamma-glutamyltransferase (gammaGT), aspartate aminotransferase (AST), sorbitoll dehydrogenase (SDH) and acid phosphatase (AF). The following changes were significantly recorded in the CL sheep in the weeks or days previous to the hemolytic crisis: higher levels of gammaGT were found on the -28th d increasing slowly but continuously until the hemolytic crisis; SDH fluctuated during the period presenting higher levels on the -28th, -14th and -7th d; AST and AF activities increased from the -14th and -7th d respectively; sharp decreases in the activities of SDH and AF at the hemolytic crisis; lower feed intake and body weight gain from the -7th d; and sheep ceased eating concentrates from the -9th d and became anoretic the day before the hemolytic crisis. Plasma copper concentration increased only the day before the hemolytic crisis. There were no changes in respiratory and heart rates, rectal temperature or rumen movements throughout the pre-hemolytic phase. The higher the amount of cumulative copper drenched, the higher was the gammaGT and AST activities. It was concluded that gammaGT followed by AST are the best enzymes to assess copper-load in sheep during the pre-hemolytic phase. Sheep fed copper-rich diets with high plasma activity of these enzymes, decreased feed consumption and subtle loss of body weight are most likely to present with a hemolytic crisis in a few days.

Topics: Acid Phosphatase; Animals; Aspartate Aminotransferases; Chemical and Drug Induced Liver Injury; Copper; Diet; gamma-Glutamyltransferase; L-Iditol 2-Dehydrogenase; Liver; Male; Poisoning; Sheep; Sheep Diseases; Time Factors

Fifteen Slovak Merino sheep were included in the experiment. The animals weighing 21-28 kg were divided into three groups per five animals. In a six-week feeding experiment the animals of group I were given 50 mg supermethrin per kg live weight per day while those of group II received 200, and from week four of the experiment 300 mg supermethrin per kg live weight per day. During the experiment changes of aspartate aminotransferase (EC 2.6.1.1), alanine aminotransferase (EC 2.6.1.2), acetylcholine esterase (EC 3.1.1.7), urea und creatinine levels in blood serum were observed. Six weeks after supermethrin treatment the sheep were slaughtered and histochemical evaluation of alkaline phosphatase (EC 3.1.3.2), acid phosphatase (EC 3.1.3.1) and non-specific esterase (EC 3.1.1.1) was carried out in liver, kidney, duodenum, jejunum and ileum. In the course of the experiment changes of the enzymatic activities of aspartate aminotransferase observed in both experimental groups of sheep were similar to those seen in the control group of animals (Tab. I). As compared to the starting values, no significant changes in the activity of alanine aminotransferase were observed in group II of the experiment and in the controls. However, a significantly decreased alanine aminotransferase activity could be seen in the blood serum of sheep of group I (Tab. II). In both experimental groups of animals no significant changes in the acetylcholine esterase could be seen (Tab. III). As compared to the starting values, no significant changes were observed in creatinine levels of the control and the 1st experimental group of sheep (Tab. IV). In the sheep of the 2nd group a temporary significant decrease (p < 0.05) in creatinine levels was seen. The dynamics of urea levels was similar to starting values in all animals throughout the experiment Tab. V). In the control group of animals (Fig. 1) the high density of reaction product of alkaline phosphatase was determined in the microvilli of enterocytes of the small intestine. In the small intestine of the animals of both experimental groups, the activity of this enzyme was shown to be located in the same zone (Fig. 2). In all experimental animals in the parenchyma of the liver and kidney no significant changes could be observed. In both experimental and control animals the high activity of acid phosphatase was demonstrated to be located especially in the cytoplasma of enterocytes. The activity of non-specific esterase was located in the c

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Female; Insecticides; Male; Poisoning; Pyrethrins; Sheep; Sheep Diseases

The experiments were carried out in mice which were divided into 4 experimental groups and a control group. In the course of the experiment SD, NADH2-tetrazolium reductase; ATP-ase, G-6-P-ase and AP were observed. It was found that acute benzene intoxication causes the disturbances in the enzymatic activities of the cells of the main segment of the nephron. The impairment of tissue respiration and oxygen phosphorylation and of active transport is due to benzene intoxication. Benzene leads to injury of the endoplasmatic reticulum in the cells of the kidney.

Topics: Acid Phosphatase; Acute Disease; Adenosine Triphosphatases; Animals; Benzene; Glucosephosphate Dehydrogenase; Kidney; Male; Mice; Poisoning; Succinate Dehydrogenase

Topics: Acetylcholinesterase; Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Brain; Cholinesterases; Demyelinating Diseases; Esterases; Glycerolphosphate Dehydrogenase; Histocytochemistry; Hydrogen Cyanide; Hydroxybutyrate Dehydrogenase; NADH, NADPH Oxidoreductases; Neuroglia; Poisoning; Rats; Succinate Dehydrogenase; Tetrazolium Salts; Thiamine; Time Factors; Transferases

Topics: Acetylcholinesterase; Acid Phosphatase; Alkaline Phosphatase; Animals; Brain; Chronic Disease; Insecticides; Kidney; Liver; Male; Muscles; Phosphoric Acids; Poisoning; Rats

Topics: Acid Phosphatase; Animals; Cyanides; Cytoplasm; Histocytochemistry; Kidney Tubules; Lysosomes; Microscopy, Electron; Mitochondria; Poisoning; Rats; Shock, Hemorrhagic

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Calcium; Cerebellum; Female; Frontal Lobe; Histocytochemistry; Magnesium; Male; Nucleotidases; Petroleum; Poisoning; Potassium; Rabbits; Sodium; Succinate Dehydrogenase

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Benzene; Histocytochemistry; Kidney; Male; Mice; Poisoning; Succinate Dehydrogenase

Topics: Acid Phosphatase; Brain; Humans; Lead Poisoning; Neurochemistry; Poisoning; Tetraethyl Lead